Molecular Dissection of Phagocytosis by Proteomic Analysis in Entamoeba histolytica
- PMID: 36833306
- PMCID: PMC9957367
- DOI: 10.3390/genes14020379
Molecular Dissection of Phagocytosis by Proteomic Analysis in Entamoeba histolytica
Abstract
Entamoeba histolytica is the enteric protozoan parasite responsible for amebiasis. Trophozoites of E. histolytica ingest human cells in the intestine and other organs, which is the hallmark of its pathogenesis. Phagocytosis and trogocytosis are pivotal biological functions for its virulence and also contribute to the proliferation of nutrient uptake from the environment. We previously elucidated the role of a variety of proteins associated with phagocytosis and trogocytosis, including Rab small GTPases, Rab effectors, including retromer, phosphoinositide-binding proteins, lysosomal hydrolase receptors, protein kinases, and cytoskeletal proteins. However, a number of proteins involved in phagocytosis and trogocytosis remain to be identified, and mechanistic details of their involvement must be elucidated at the molecular level. To date, a number of studies in which a repertoire of proteins associated with phagosomes and potentially involved in phagocytosis have been conducted. In this review, we revisited all phagosome proteome studies we previously conducted in order to reiterate information on the proteome of phagosomes. We demonstrated the core set of constitutive phagosomal proteins and also the set of phagosomal proteins recruited only transiently or in condition-dependent fashions. The catalogs of phagosome proteomes resulting from such analyses can be a useful source of information for future mechanistic studies as well as for confirming or excluding a possibility of whether a protein of interest in various investigations is likely or is potentially involved in phagocytosis and phagosome biogenesis.
Keywords: E. histolytica; phagocytosis; proteomics.
Conflict of interest statement
The authors declare no conflict of interest. The funders had no role in the design of this study, in the collection, analyses, or interpretation of data, in the writing of the manuscript, or in the decision to publish the results.
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References
-
- Nakada-tsukui K., Watanabe N., Shibata K., Wahyuni R., Miyamoto E., Nozaki T. Proteomic analysis of Atg8-dependent recruitment of phagosomal proteins in the enteric protozoan parasite Entamoeba histolytica. Front. Cell Infect. Microbiol. 2022;12:1–14. doi: 10.3389/fcimb.2022.961645. - DOI - PMC - PubMed
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